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Siglec-1 His Tag Protein, Human
Siglec-1 His Tag Protein, Human
Origin of place Singapore
Model UA010865-100μg
Supplier ANT BIO PTE.LTD.
Price 604
Hits 0
Updated 8/25/2025
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Product Specification


SpeciesHuman
SynonymsSialic acid-binding Ig-like lectin 1, Siglec-1, CD169
AccessionQ9BZZ2-1
Amino Acid SequenceSer20-Gln1641, with C-terminal His
Expression SystemHEK293
Molecular Weight175-190kDa (Reducing)
Purity>95% by SDS-PAGE
Endotoxin<0.1EU/μg
ConjugationUnconjugated
TagHis Tag
Physical AppearanceLyophilized Powder
Storage BufferPBS, pH7.4.
ReconstitutionReconstitute at 0.1-1 mg/ml according to the size in ultrapure water after rapid centrifugation.
Stability & Storage· 12 months from date of receipt, lyophilized powder stored at -20 to -80℃.
· 3 months, -20 to -80℃ under sterile conditions after reconstitution.
· 1 week, 2 to 8℃ under sterile conditions after reconstitution.
· Please avoid repeated freeze-thaw cycles.
Reference

Crocker P.R., Paulson J.C., Varki A. Siglecs and their roles in the immune system. Nat. Rev. Immunol. 2007; 7:255–266.
Hartnell A., Steel J., Turley H., Jones M., Jackson D.G., Crocker P.R. Characterization of human sialoadhesin, a sialic acid binding receptor expressed by resident and inflammatory macrophage populations. Blood. 2001; 97:288–296.
Puryear W.B., Akiyama H., Geer S.D., Ramirez N.P., Yu X., Reinhard B.M., Gummuluru S. Interferon-inducible mechanism of dendritic cell-mediated HIV-1 dissemination is dependent on Siglec-1/CD169. PLoS Pathog. 2013; 9: e1003291.
Rempel H., Calosing C., Sun B., Pulliam L. Sialoadhesin expressed on IFN-induced monocytes binds HIV-1 and enhances infectivity. PLoS ONE. 2008; 3: e1967.

Background

Human Siglec-1, a 175-185 kDa glycoprotein, also known as sialoadhesin or CD169, selectively binds to 2,3-linked sialic acid residues. Siglec-1 is a type I transmembrane lectin with an amino-terminal V-set domain that interacts with sialylated ligands, preferentially N-acetylneuraminic acid (Neu5Ac) in an α2–3 linkage. Moreover, as Siglec-1 contains 16 Ig-like C2-type extracellular domains that separate the ligand-binding site from the cell surface, it is available for interaction with external ligands and not bound in cis to cell-surface molecules, which is what usually happens with shorter Siglecs that are also expressed by DCs. Siglec-1 is a receptor codified by an interferon-stimulated gene and is therefore potently upregulated on distinct human DCs, monocytes, and macrophages when these cells sense type I interferons (IFNs) such as IFNα.

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